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    Plasminogen activator/coagulase gene of Yersinia pestis is responsible for degradation of plasmid-encoded outer membrane proteins

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    Authors
    Sodeinde, Olanrewaju A.
    Sample, Allen K.
    Brubaker, Robert R.
    Goguen, Jon D.
    UMass Chan Affiliations
    Department of Molecular Genetics and Microbiology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1988-10-01
    Keywords
    Bacterial Outer Membrane Proteins; Coagulase; DNA Mutational Analysis; DNA Transposable Elements; Genes, Bacterial; Immunosorbent Techniques; Molecular Weight; Plasmids; Plasminogen Activators; Yersinia pestis
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC259639/
    Abstract
    The related family of virulence plasmids found in the three major pathogens of the genus Yersinia all have the ability to encode a set of outer membrane proteins. In Y. enterocolitica and Y. pseudotuberculosis, these proteins are major constituents of the outer membrane when their synthesis is fully induced. In contrast, they have been difficult to detect in Y. pestis. It has recently been established that Y. pestis does synthesize these proteins, but that they are rapidly degraded due to some activity determined by the 9.5-kilobase plasmid commonly found in Y. pestis strains. We show that mutations in the pla gene of this plasmid, which encodes both the plasminogen activator and coagulase activities, blocked this degradation. A cloned 1.4-kilobase DNA fragment carrying pla was also sufficient to cause degradation in the absence of the 9.5-kilobase plasmid.
    Source

    Infect Immun. 1988 Oct;56(10):2749-52.

    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32573
    PubMed ID
    2843471
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